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PKC phosphorylates KCNQ2. 24 / 26
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"Gq/11 coupled receptors result in the hydrolysis of PIP2 into diacylglycerol (DAG) and inositol triphosphate (IP3), leading to the activation of PKC which phosphorylates Kv7.2 subunit."
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"Previous work showed AKAP79 to co-precipitate with KCNQ2 channels (Cooper et al., 2000), and to facilitate PKC phosphorylation of KCNQ2 channels (Hoshi et al., 2003)."
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"PKC-dependent phosphorylation of Kv7.2 at Ser 534 and Ser 541 sites facilitates receptor-induced inhibition of channel activity ( Hoshi et al., 2003 )."
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"Activated PKC phosphorylates the C-terminus in the calmodulin (CaM) binding site of the Kv7.2 subunit assisted by A-kinase-anchoring protein AKAP79/150."
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"This maintains PKC where it can optimally respond to activating signals from the m1 receptor and preferentially phosphorylate the KCNQ2 subunit."
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"In neurons muscarinic agonists mobilize an AKAP79-anchored pool of PKC that phosphorylates the KCNQ2 subunit of the M channel."
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"Muscarinic agonists such as acetylcholine mobilize an anchored pool of PKC that phosphorylates the KCNQ2 subunit of the M channel on Ser 541 to decrease potassium permeability ( xref )."
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"Previous work showed AKAP79 to co-precipitate with KCNQ2 channels (Cooper et al., 2000), and to facilitate PKC phosphorylation of KCNQ2 channels (Hoshi et al., 2003)."
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"In response to muscarinic agonists, PKC phosphorylates the KCNQ2 subunit and inhibits potassium current through the M channel, an important step in regulating neuronal excitability."
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"PKC phosphorylation of the KCNQ2 channel subunit induces dissociation of calmodulin from the M-channel complex."
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"Recently, phosphorylation of KCNQ2 by protein kinase C (PKC) has been shown to dissociate CaM from KCNQ2 channels, leading to a reduced affinity to PIP 2 and suppression of M-current XREF_BIBR."
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"Recent work indicates that protein kinase C (PKC) phosphorylation of the KCNQ2 subunit reduces the affinity for its PIP 2 binding and activities."
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"Recent work indicates that protein kinase C (PKC) phosphorylation of the KCNQ2 subunit reduces the affinity for its PIP 2 binding and activities."
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"Another mechanism is mediated by protein kinase C (PKC), which phosphorylates the KV7.2 subunit to reduce PIP2 efficacy."
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"When Gq-coupled receptors are activated, Kv7 anchored PKC phosphorylates Kv7.2 subunits, which reduces the affinity of Kv7.2 toward phosphatidylinositol 4,5-bisphosphate (PIP2) and results in a loss of PIP2 from Kv7 channels (Hoshi et al., 2003; Kosenko et al., 2012)."
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"By simultaneously binding the KCNQ2 channel subunit and protein kinase C (PKC), AKAP79 facilitates the PKC-dependent phosphorylation of KCNQ2 and the subsequent inhibition of the M current ( Hoshi et [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The in vitro kinase assay showed that KCNQ2 subunits of M channel can be phosphorylated by PKC."
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"By simultaneously binding the KCNQ2 channel subunit and protein kinase C (PKC), AKAP79 facilitates the PKC-dependent phosphorylation of KCNQ2 and the subsequent inhibition of the M current ( Hoshi et [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
20188664
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"PKC phosphorylation of the KCNQ2 channel subunit induces dissociation of calmodulin from the M and channel complex."
22643219
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"Another mechanism is mediated by protein kinase C (PKC), which phosphorylates the KV7.2 subunit to reduce PIP2 efficacy."
31238068
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"Recently, phosphorylation of KCNQ2 by protein kinase C (PKC) has been shown to dissociate CaM from KCNQ2 channels, leading to a reduced affinity to PIP 2 and suppression of M-current xref ."
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"AKAP79-bound CKAR should be a good proxy for PKC phosphorylation of AKAP79-bound KCNQ2."
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"In response to muscarinic agonists, PKC phosphorylates the KCNQ2 subunit and inhibits potassium current through the M channel, an important step in regulating neuronal excitability."
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"The molecular pathways leading to M-current inhibition include pKC phosphorylation of the Kv7.2 subunits, dissociation of CaM from the channel and a consequent reduced affinity towards PIP (Kosenko et al., 2012)."
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